EC Number   |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Reference |
|---|
    2.1.2.1 | -999 |
- |
more |
- |
441405, 441407, 441408, 441410, 441412, 441413, 441420 |
| 2.1.2.1 | -999 |
- |
more |
allosteric kinetics |
441403 |
| 2.1.2.1 | -999 |
- |
more |
kinetic analysis of ternary complex mechanism, determination of ligand binding, transient, single-turnover and bi-substrate steady-state kinetics, detailed overview. The enzyme can bind first to either L-serine or tetrahydrofolate. The dissociation constants for the enzyme-L-serine and enzyme-tetrahydrofolate complexes are 0.18 mM and 0.35 mM, respectively. The kinetic mechanism of PvSHMT occurs via a random-order model and glycine formation is the rate-limiting step of the enzyme reaction |
736499 |
| 2.1.2.1 | -999 |
- |
more |
pH-dependence of kinetic parameters |
441420 |
| 2.1.2.1 | -999 |
- |
more |
steady-state kinetics |
736646 |
| 2.1.2.1 | -999 |
- |
more |
steady-state kinetics, overview |
736084 |
| 2.1.2.1 | 0.002 |
- |
(6S)-tetrahydrofolate |
pH 7.2, 37°C |
726831 |
| 2.1.2.1 | 0.003 |
- |
tetrahydrofolate |
mutant enzyme H135A, in the presence of NADP+, at pH 3.0 and 30°C |
755905 |
| 2.1.2.1 | 0.0031 |
- |
tetrahydrofolate |
mutant enzyme H119A, in the presence of NADP+, at pH 3.0 and 30°C |
755905 |
| 2.1.2.1 | 0.0037 |
- |
tetrahydrofolate |
mutant L474F |
671589 |
